Evidence map›Paper›PMID 26354862›Full record

ArticleNucleic acids research2015

Nucleolin stabilizes G-quadruplex structures folded by the LTR promoter and silences HIV-1 viral transcription.

Elena Tosoni, Ilaria Frasson, Matteo Scalabrin, Rosalba Perrone, Elena Butovskaya, Matteo Nadai, Giorgio Palù, Dan Fabris, Sara N Richter

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
5.9field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

84 citing papers in PubMed, 149 citations in OpenAlex.

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  19. Crosstalk between G-quadruplex and ROS.Cell death & disease · 2023
    Review
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24 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 2 countries.

Elena TosoniDepartment of Molecular Medicine, University of Padua, via Gabelli 63, 35121 Padua, Italy.
Ilaria FrassonDepartment of Molecular Medicine, University of Padua, via Gabelli 63, 35121 Padua, Italy.
Matteo ScalabrinDepartment of Molecular Medicine, University of Padua, via Gabelli 63, 35121 Padua, Italy The RNA Institute, University at Albany-SUNY, Albany, NY 12222, USA.
Rosalba PerroneDepartment of Molecular Medicine, University of Padua, via Gabelli 63, 35121 Padua, Italy.
Elena ButovskayaDepartment of Molecular Medicine, University of Padua, via Gabelli 63, 35121 Padua, Italy.
Matteo NadaiDepartment of Molecular Medicine, University of Padua, via Gabelli 63, 35121 Padua, Italy.
Giorgio PalùDepartment of Molecular Medicine, University of Padua, via Gabelli 63, 35121 Padua, Italy.
Dan FabrisThe RNA Institute, University at Albany-SUNY, Albany, NY 12222, USA.
Sara N RichterDepartment of Molecular Medicine, University of Padua, via Gabelli 63, 35121 Padua, Italy sara.richter@unipd.it.
University of Padua · ITUniversity at Albany, State University of New York · US

Funding

Structural determinants of HIV-1 5'-UTR riboswitch and NC actuation by MS3DR01GM064328 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI FABRIS, DANIELE · 2001 to 2013
$3.8M
European Research Council 615879NIGMS NIH HHS GM064328
6 · The paper itself

Abstract

Folding of the LTR promoter into dynamic G-quadruplex conformations has been shown to suppress its transcriptional activity in HIV-1. Here we sought to identify the proteins that control the folding of this region of proviral genome by inducing/stabilizing G-quadruplex structures. The implementation of electrophorethic mobility shift assay and pull-down experiments coupled with mass spectrometric analysis revealed that the cellular protein nucleolin is able to specifically recognize G-quadruplex structures present in the LTR promoter. Nucleolin recognized with high affinity and specificity the majority, but not all the possible G-quadruplexes folded by this sequence. In addition, it displayed greater binding preference towards DNA than RNA G-quadruplexes, thus indicating two levels of selectivity based on the sequence and nature of the target. The interaction translated into stabilization of the LTR G-quadruplexes and increased promoter silencing activity; in contrast, disruption of nucleolin binding in cells by both siRNAs and a nucleolin binding aptamer greatly increased LTR promoter activity. These data indicate that nucleolin possesses a specific and regulated activity toward the HIV-1 LTR promoter, which is mediated by G-quadruplexes. These observations provide new essential insights into viral transcription and a possible low mutagenic target for antiretroviral therapy.

Indexed as

Gene SilencingG-QuadruplexesHIV Long Terminal RepeatPromoter Regions, GeneticTranscription, GeneticCell LineHIV-1HumansNucleolinPhosphoproteinsRNA-Binding ProteinsNucleolinPhosphoproteinsRNA-Binding Proteins

Identifiers

PMID26354862
PMCPMC4605322
OpenAlexW1862469243

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.